Rab41 Is a Novel Regulator of Golgi Apparatus Organization That Is Needed for ER-To-Golgi Trafficking and Cell Growth

@article{Liu2013Rab41IA,
  title={Rab41 Is a Novel Regulator of Golgi Apparatus Organization That Is Needed for ER-To-Golgi Trafficking and Cell Growth},
  author={Shijie Liu and Lauren Hunt and Brian Storrie},
  journal={PLoS ONE},
  year={2013},
  volume={8}
}
Background The 60+ members of the mammalian Rab protein family group into subfamilies postulated to share common functionality. The Rab VI subfamily contains 5 Rab proteins, Rab6a/a’, Rab6b, Rab6c and Rab41. High-level knockdown of Rab6a/a’ has little effect on the tightly organized Golgi ribbon in HeLa cells as seen by fluorescence microscopy. In striking contrast, we found Rab41 was strongly required for normal Golgi ribbon organization. Methods/Results Treatment of HeLa cells with Rab41… 
How Rab proteins determine Golgi structure.
How Do Rab Proteins Determine Golgi Structure?
TLDR
The balance between minus-and plus-end directed motor recruitment may well be the major Rab-dependent factor in Golgi ribbon organization.
Identification of Rab41/6d Effectors Provides an Explanation for the Differential Effects of Rab41/6d and Rab6a/a' on Golgi Organization
TLDR
Dynactin 6, a subunit of dynactin complex, the minus-end-directed, dynein motor, provides a sufficient molecular basis to explain the active role of Rab41/6d in maintaining Golgi ribbon organization while syntaxin 8 contributes more indirectly to Golgi positioning.
Multiple Roles of Rab GTPases at the Golgi.
  • C. Progida
  • Biology
    Results and problems in cell differentiation
  • 2019
TLDR
This chapter will summarize the different roles of Rab GTPases at the Golgi, both as regulators of membrane transport, scaffold, and tethering proteins and in preserving the structure and function of this organelle.
Rab proteins as major determinants of the Golgi complex structure
TLDR
Through interactions with a variety of effectors that include molecular motors, tethering complexes, scaffolding proteins and lipid kinases, Rab family GTP-ases play an important role in maintaining Golgi architecture.
Rab6b localizes to the Golgi complex in murine macrophages and promotes tumor necrosis factor release in response to mycobacterial infection
TLDR
It is shown that Rab6b is expressed by primary mouse macrophages, where it localized to the Golgi complex, and is identified as a positive regulator of M. bovis BCG‐infected macrophage TNF trafficking and secretion.
Golgi Apparatus: A Potential Therapeutic Target for Autophagy-Associated Neurological Diseases
TLDR
Target therapies aimed at protecting the Golgi or regulating Golgi proteins might prevent or ameliorate autophagy-related neurological diseases, as well as investigate the potential application of Golgi therapy in autophagic-based neurological diseases.
Ubiquitination-Dependent Regulation of Small GTPases in Membrane Trafficking: From Cell Biology to Human Diseases
TLDR
An in-depth understanding of the molecular mechanisms by which ubiquitination regulates small GTPases can provide novel insights into the membrane trafficking process, which knowledge is valuable for the development of more effective and specific therapeutics for membrane trafficking-related human diseases.
...
...

References

SHOWING 1-10 OF 38 REFERENCES
Rab18 and Rab43 have key roles in ER-Golgi trafficking
TLDR
This study is the first comprehensive application of large-scale proteomics to the cell biology of small GTPases of the secretory pathway to Golgi or intra-Golgi localization, dominant-negative and overexpression phenotypes.
Rab33b and Rab6 are Functionally Overlapping Regulators of Golgi Homeostasis and Trafficking
TLDR
The first evidence that Rab33b and Rab6 act to coordinate a major intra‐Golgi retrograde trafficking pathway is provided, which may have parallels with Rab conversion/cascade events that regulate endosome, phagosome and exocytic processes.
Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells
TLDR
It is indicated that Rab1 and Rab43 are key Rabs required for the biogenesis and maintenance of a functional Golgi structure, and suggest that other Rabs acting at the Golgi complex are likely to be functionally redundant.
Are Rab proteins the link between Golgi organization and membrane trafficking?
TLDR
Speculation on the essential role of Rab proteins in Golgi organization and protein transport is speculated based on evidence from both yeast and mammalian cells.
Regulation of microtubule-dependent recycling at the trans-Golgi network by Rab6A and Rab6A'.
TLDR
Evidence is presented that a recycling pathway operates at the level of the trans-Golgi linking directly to the ER, which would be the preferred route for both toxins and resident Golgi proteins.
Rab6 regulates both ZW10/RINT-1 and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis.
TLDR
It is concluded that Rab6 regulates distinct Golgi trafficking pathways involving two separate protein complexes: ZW10/RINT-1 and COG.
Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress.
TLDR
Golgi cisternal rabs, and in particular rab6a, are regulators of the Golgi response to stress and presumably the molecular targets of stress-activated signaling pathway(s), and it is concluded that rab 6a can regulate select microtubule-independent processes as well as micro Tubule-dependent processes.
The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus.
TLDR
The results suggest a cell-type specific role for Rab6B in retrograde membrane traffic at the level of the Golgi complex, and the GTP-bound form of Rab6b Q72L does interact with all known Rab6A effectors, including Rabkinesin-6.
The small GTP-binding protein rab6p is distributed from medial Golgi to the trans-Golgi network as determined by a confocal microscopic approach.
TLDR
The results show that the small GTP-binding protein rab6p is distributed from medial Golgi to TGN along the exocytic pathway.
The small GTP-binding protein rab6 functions in intra-Golgi transport
TLDR
Overexpression of both rab6 Q72L and rab6 T27N altered the morphology of the Golgi apparatus as well as that of the TGN, as assessed at the immunofluorescence level with several markers, indicating that rab6 controls intra-Golgi transport, either acting as an inhibitor in anterograde transport or as a positive regulator of retrograde transport.
...
...